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Structure-based statistical analysis of transmembrane helices

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Structure-based statistical analysis of transmembrane helices

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dc.contributor.author Baeza Delgado, Carlos
dc.contributor.author Martí Renom, Marc A.
dc.contributor.author Mingarro Muñoz, Ismael
dc.date.accessioned 2014-03-28T12:49:55Z
dc.date.available 2014-03-28T12:49:55Z
dc.date.issued 2013
dc.identifier.citation Baeza Delgado, Carlos Marti Renom, Marc A. Mingarro Muñoz, Ismael 2013 Structure-based statistical analysis of transmembrane helices European Biophysics Journal With Biophysics Letters 42 2-3 199 207
dc.identifier.uri http://hdl.handle.net/10550/33749
dc.description.abstract Recent advances in determination of the high-resolution structure of membrane proteins now enable analysis of the main features of amino acids in transmembrane (TM) segments in comparison with amino acids in water-soluble helices. In this work, we conducted a large-scale analysis of the prevalent locations of amino acids by using a data set of 170 structures of integral membrane proteins obtained from the MPtopo database and 930 structures of water-soluble helical proteins obtained from the protein data bank. Large hydrophobic amino acids (Leu, Val, Ile, and Phe) plus Gly were clearly prevalent in TM helices whereas polar amino acids (Glu, Lys, Asp, Arg, and Gln) were less frequent in this type of helix. The distribution of amino acids along TM helices was also examined. As expected, hydrophobic and slightly polar amino acids are commonly found in the hydrophobic core of the membrane whereas aromatic (Trp and Tyr), Pro, and the hydrophilic amino acids (Asn, His, and Gln) occur more frequently in the interface regions. Charged amino acids are also statistically prevalent outside the hydrophobic core of the membrane, and whereas acidic amino acids are frequently found at both cytoplasmic and extra-cytoplasmic interfaces, basic amino acids cluster at the cytoplasmic interface. These results strongly support the experimentally demonstrated biased distribution of positively charged amino acids (that is, the so-called the positive-inside rule) with structural data.
dc.relation.ispartof European Biophysics Journal With Biophysics Letters, 2013, vol. 42, num. 2-3, p. 199-207
dc.subject Biofísica
dc.subject Seqüència d'aminoàcids
dc.title Structure-based statistical analysis of transmembrane helices
dc.type journal article es_ES
dc.date.updated 2014-03-28T12:49:55Z
dc.identifier.doi 10.1007/s00249-012-0813-9
dc.identifier.idgrec 081118
dc.rights.accessRights open access es_ES
dc.identifier.url 10.1007/s00249-012-0813-9

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